User:Ralf Stephan/Sandbox 2
From Proteopedia
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== Classification and catalytic center == | == Classification and catalytic center == | ||
| - | Thermolysin is a well researched metallo protease containing <scene name='User:Ralf_Stephan/Sandbox_2/ | + | Thermolysin is a well researched metallo protease containing <scene name='User:Ralf_Stephan/Sandbox_2/Zinc/1'>zinc</scene> and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif. |
| - | <scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/2'>Glu-166, His-142 and -146 are grouped around the zinc atom</scene>, holding it fast, while Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231 stabilize the substrate. | + | <scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/2'>Glu-166, His-142 and -146 are grouped around the zinc atom</scene>, holding it fast, while <scene name='User:Ralf_Stephan/Sandbox_2/Res_orange/1'>Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231</scene> stabilize the substrate. |
==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ||
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==Reference== | ==Reference== | ||
| - | On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131760 16131760] | + | *On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131760 16131760] |
| + | * Matthews, BW. (1988): ''Structural basis of the action of thermolysin and related zinc peptidases''. In: ''Acc. Chem. Res.'' '''21'''(9); 333–340; http://dx.doi.org/10.1021/ar00153a003 | ||
| + | * Pelmenschikov, V. ''et al.'' (2002): ''A theoretical study of the mechanism for peptide hydrolysis by thermolysin''. ''J Biol Inorg Chem.'' '''7'''(3); 284–98; PMID:11935352; http://dx.doi.org/10.1007/s007750100295 | ||
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[[Category: Bacillus thermoproteolyticus]] | [[Category: Bacillus thermoproteolyticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Revision as of 10:27, 7 February 2009
Contents |
Classification and catalytic center
Thermolysin is a well researched metallo protease containing and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif. , holding it fast, while stabilize the substrate.
On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
Template:ABSTRACT PUBMED 16131760
About this Structure
2A7G is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.
Reference
- On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760
- Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; http://dx.doi.org/10.1021/ar00153a003
- Pelmenschikov, V. et al. (2002): A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 7(3); 284–98; PMID:11935352; http://dx.doi.org/10.1007/s007750100295
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